anti-gfp Search Results


95
Miltenyi Biotec anti gfp magnetic microbeads
Anti Gfp Magnetic Microbeads, supplied by Miltenyi Biotec, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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MedChemExpress anti gfp beads
Anti Gfp Beads, supplied by MedChemExpress, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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NeuroMab anti gfp antibody
Anti Gfp Antibody, supplied by NeuroMab, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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St Johns Laboratory mouse monoclonal anti gfp antibody
Filling and decoration of TRAP-cage. (a) Native PAGE gels showing purified TRAP-cage incubated with His-tagged <t>GFP(-21)</t> after passing through a Ni-NTA column in the absence (−TCEP) or presence (+TCEP) of TCEP. Lane 1: GFP(-21) positive control; 2: molecular weight marker for native PAGE; 3: empty TRAP-cage; 4: input [TRAP-cage with GFP(-21)]; 5 and 8: flow through; 6 and 9: wash; and 7 and 10: elution. Collected fractions were stained for protein (left) or analyzed by fluorescence detection (right, exct. 488 nm). The GFP signal visible in lane 10 of the right-side gel likely reflects GFP still bound to a TRAP ring. (b) Western blot of the gel in (a): collected fractions were subjected to SDS-PAGE followed by western blot <t>with</t> <t>anti-GFP</t> detection. Lane 1: GFP(-21) positive control; 2: molecular weight marker for SDS-PAGE; 3: empty TRAP-cage; 4: input (TRAP-cage with GFP); 5 and 8: flow through; 6 and 9: wash; and 7 and 10: elution. (c) Native PAGE gels showing encapsulation of GFP(-21) by unmodified TRAP-cage or TRAP-cage externally modified with Alexa-647 and PTD4. Lane 1: TRAP-cage with GFP(-21); 2: TRAP-cage with GFP(-21) decorated with Alexa-647; 3: TRAP-cage with GFP(-21) decorated with Alexa-647 and PTD4; and 4: molecular weight marker for native PAGE. Gels were stained for protein (upper panel) and analyzed by fluorescence detection of GFP (middle panel, exct. 488 nm) and Alexa-647 (bottom panel, exct. 647). Gels were imaged using a Biorad Chemidoc detector. (d) Negative stain TEM of TRAP-cage with GFP(-21) (left panel); TRAP-cage with GFP(-21) decorated with Alexa-647 (middle panel); and TRAP-cage with GFP(-21) decorated with Alexa-647 and PTD4 (right panel).
Mouse Monoclonal Anti Gfp Antibody, supplied by St Johns Laboratory, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Rockland Immunochemicals goat anti gfp hrp
Filling and decoration of TRAP-cage. (a) Native PAGE gels showing purified TRAP-cage incubated with His-tagged <t>GFP(-21)</t> after passing through a Ni-NTA column in the absence (−TCEP) or presence (+TCEP) of TCEP. Lane 1: GFP(-21) positive control; 2: molecular weight marker for native PAGE; 3: empty TRAP-cage; 4: input [TRAP-cage with GFP(-21)]; 5 and 8: flow through; 6 and 9: wash; and 7 and 10: elution. Collected fractions were stained for protein (left) or analyzed by fluorescence detection (right, exct. 488 nm). The GFP signal visible in lane 10 of the right-side gel likely reflects GFP still bound to a TRAP ring. (b) Western blot of the gel in (a): collected fractions were subjected to SDS-PAGE followed by western blot <t>with</t> <t>anti-GFP</t> detection. Lane 1: GFP(-21) positive control; 2: molecular weight marker for SDS-PAGE; 3: empty TRAP-cage; 4: input (TRAP-cage with GFP); 5 and 8: flow through; 6 and 9: wash; and 7 and 10: elution. (c) Native PAGE gels showing encapsulation of GFP(-21) by unmodified TRAP-cage or TRAP-cage externally modified with Alexa-647 and PTD4. Lane 1: TRAP-cage with GFP(-21); 2: TRAP-cage with GFP(-21) decorated with Alexa-647; 3: TRAP-cage with GFP(-21) decorated with Alexa-647 and PTD4; and 4: molecular weight marker for native PAGE. Gels were stained for protein (upper panel) and analyzed by fluorescence detection of GFP (middle panel, exct. 488 nm) and Alexa-647 (bottom panel, exct. 647). Gels were imaged using a Biorad Chemidoc detector. (d) Negative stain TEM of TRAP-cage with GFP(-21) (left panel); TRAP-cage with GFP(-21) decorated with Alexa-647 (middle panel); and TRAP-cage with GFP(-21) decorated with Alexa-647 and PTD4 (right panel).
Goat Anti Gfp Hrp, supplied by Rockland Immunochemicals, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Rockland Immunochemicals goat anti gfp fitc
Filling and decoration of TRAP-cage. (a) Native PAGE gels showing purified TRAP-cage incubated with His-tagged <t>GFP(-21)</t> after passing through a Ni-NTA column in the absence (−TCEP) or presence (+TCEP) of TCEP. Lane 1: GFP(-21) positive control; 2: molecular weight marker for native PAGE; 3: empty TRAP-cage; 4: input [TRAP-cage with GFP(-21)]; 5 and 8: flow through; 6 and 9: wash; and 7 and 10: elution. Collected fractions were stained for protein (left) or analyzed by fluorescence detection (right, exct. 488 nm). The GFP signal visible in lane 10 of the right-side gel likely reflects GFP still bound to a TRAP ring. (b) Western blot of the gel in (a): collected fractions were subjected to SDS-PAGE followed by western blot <t>with</t> <t>anti-GFP</t> detection. Lane 1: GFP(-21) positive control; 2: molecular weight marker for SDS-PAGE; 3: empty TRAP-cage; 4: input (TRAP-cage with GFP); 5 and 8: flow through; 6 and 9: wash; and 7 and 10: elution. (c) Native PAGE gels showing encapsulation of GFP(-21) by unmodified TRAP-cage or TRAP-cage externally modified with Alexa-647 and PTD4. Lane 1: TRAP-cage with GFP(-21); 2: TRAP-cage with GFP(-21) decorated with Alexa-647; 3: TRAP-cage with GFP(-21) decorated with Alexa-647 and PTD4; and 4: molecular weight marker for native PAGE. Gels were stained for protein (upper panel) and analyzed by fluorescence detection of GFP (middle panel, exct. 488 nm) and Alexa-647 (bottom panel, exct. 647). Gels were imaged using a Biorad Chemidoc detector. (d) Negative stain TEM of TRAP-cage with GFP(-21) (left panel); TRAP-cage with GFP(-21) decorated with Alexa-647 (middle panel); and TRAP-cage with GFP(-21) decorated with Alexa-647 and PTD4 (right panel).
Goat Anti Gfp Fitc, supplied by Rockland Immunochemicals, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Rockland Immunochemicals anti gfp hrp
Filling and decoration of TRAP-cage. (a) Native PAGE gels showing purified TRAP-cage incubated with His-tagged <t>GFP(-21)</t> after passing through a Ni-NTA column in the absence (−TCEP) or presence (+TCEP) of TCEP. Lane 1: GFP(-21) positive control; 2: molecular weight marker for native PAGE; 3: empty TRAP-cage; 4: input [TRAP-cage with GFP(-21)]; 5 and 8: flow through; 6 and 9: wash; and 7 and 10: elution. Collected fractions were stained for protein (left) or analyzed by fluorescence detection (right, exct. 488 nm). The GFP signal visible in lane 10 of the right-side gel likely reflects GFP still bound to a TRAP ring. (b) Western blot of the gel in (a): collected fractions were subjected to SDS-PAGE followed by western blot <t>with</t> <t>anti-GFP</t> detection. Lane 1: GFP(-21) positive control; 2: molecular weight marker for SDS-PAGE; 3: empty TRAP-cage; 4: input (TRAP-cage with GFP); 5 and 8: flow through; 6 and 9: wash; and 7 and 10: elution. (c) Native PAGE gels showing encapsulation of GFP(-21) by unmodified TRAP-cage or TRAP-cage externally modified with Alexa-647 and PTD4. Lane 1: TRAP-cage with GFP(-21); 2: TRAP-cage with GFP(-21) decorated with Alexa-647; 3: TRAP-cage with GFP(-21) decorated with Alexa-647 and PTD4; and 4: molecular weight marker for native PAGE. Gels were stained for protein (upper panel) and analyzed by fluorescence detection of GFP (middle panel, exct. 488 nm) and Alexa-647 (bottom panel, exct. 647). Gels were imaged using a Biorad Chemidoc detector. (d) Negative stain TEM of TRAP-cage with GFP(-21) (left panel); TRAP-cage with GFP(-21) decorated with Alexa-647 (middle panel); and TRAP-cage with GFP(-21) decorated with Alexa-647 and PTD4 (right panel).
Anti Gfp Hrp, supplied by Rockland Immunochemicals, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/anti-gfp/GFP+Antibody+Peroxidase+Conjugate/pmc02870955-99-15-16
Average 95 stars, based on 1 article reviews
anti gfp hrp - by Bioz Stars, 2026-10
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Rockland Immunochemicals alkaline phosphatase
Filling and decoration of TRAP-cage. (a) Native PAGE gels showing purified TRAP-cage incubated with His-tagged <t>GFP(-21)</t> after passing through a Ni-NTA column in the absence (−TCEP) or presence (+TCEP) of TCEP. Lane 1: GFP(-21) positive control; 2: molecular weight marker for native PAGE; 3: empty TRAP-cage; 4: input [TRAP-cage with GFP(-21)]; 5 and 8: flow through; 6 and 9: wash; and 7 and 10: elution. Collected fractions were stained for protein (left) or analyzed by fluorescence detection (right, exct. 488 nm). The GFP signal visible in lane 10 of the right-side gel likely reflects GFP still bound to a TRAP ring. (b) Western blot of the gel in (a): collected fractions were subjected to SDS-PAGE followed by western blot <t>with</t> <t>anti-GFP</t> detection. Lane 1: GFP(-21) positive control; 2: molecular weight marker for SDS-PAGE; 3: empty TRAP-cage; 4: input (TRAP-cage with GFP); 5 and 8: flow through; 6 and 9: wash; and 7 and 10: elution. (c) Native PAGE gels showing encapsulation of GFP(-21) by unmodified TRAP-cage or TRAP-cage externally modified with Alexa-647 and PTD4. Lane 1: TRAP-cage with GFP(-21); 2: TRAP-cage with GFP(-21) decorated with Alexa-647; 3: TRAP-cage with GFP(-21) decorated with Alexa-647 and PTD4; and 4: molecular weight marker for native PAGE. Gels were stained for protein (upper panel) and analyzed by fluorescence detection of GFP (middle panel, exct. 488 nm) and Alexa-647 (bottom panel, exct. 647). Gels were imaged using a Biorad Chemidoc detector. (d) Negative stain TEM of TRAP-cage with GFP(-21) (left panel); TRAP-cage with GFP(-21) decorated with Alexa-647 (middle panel); and TRAP-cage with GFP(-21) decorated with Alexa-647 and PTD4 (right panel).
Alkaline Phosphatase, supplied by Rockland Immunochemicals, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Rockland Immunochemicals biotinylated polyclonal goat anti gfp
Filling and decoration of TRAP-cage. (a) Native PAGE gels showing purified TRAP-cage incubated with His-tagged <t>GFP(-21)</t> after passing through a Ni-NTA column in the absence (−TCEP) or presence (+TCEP) of TCEP. Lane 1: GFP(-21) positive control; 2: molecular weight marker for native PAGE; 3: empty TRAP-cage; 4: input [TRAP-cage with GFP(-21)]; 5 and 8: flow through; 6 and 9: wash; and 7 and 10: elution. Collected fractions were stained for protein (left) or analyzed by fluorescence detection (right, exct. 488 nm). The GFP signal visible in lane 10 of the right-side gel likely reflects GFP still bound to a TRAP ring. (b) Western blot of the gel in (a): collected fractions were subjected to SDS-PAGE followed by western blot <t>with</t> <t>anti-GFP</t> detection. Lane 1: GFP(-21) positive control; 2: molecular weight marker for SDS-PAGE; 3: empty TRAP-cage; 4: input (TRAP-cage with GFP); 5 and 8: flow through; 6 and 9: wash; and 7 and 10: elution. (c) Native PAGE gels showing encapsulation of GFP(-21) by unmodified TRAP-cage or TRAP-cage externally modified with Alexa-647 and PTD4. Lane 1: TRAP-cage with GFP(-21); 2: TRAP-cage with GFP(-21) decorated with Alexa-647; 3: TRAP-cage with GFP(-21) decorated with Alexa-647 and PTD4; and 4: molecular weight marker for native PAGE. Gels were stained for protein (upper panel) and analyzed by fluorescence detection of GFP (middle panel, exct. 488 nm) and Alexa-647 (bottom panel, exct. 647). Gels were imaged using a Biorad Chemidoc detector. (d) Negative stain TEM of TRAP-cage with GFP(-21) (left panel); TRAP-cage with GFP(-21) decorated with Alexa-647 (middle panel); and TRAP-cage with GFP(-21) decorated with Alexa-647 and PTD4 (right panel).
Biotinylated Polyclonal Goat Anti Gfp, supplied by Rockland Immunochemicals, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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biotinylated polyclonal goat anti gfp - by Bioz Stars, 2026-10
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Rockland Immunochemicals goat anti gfp
Filling and decoration of TRAP-cage. (a) Native PAGE gels showing purified TRAP-cage incubated with His-tagged <t>GFP(-21)</t> after passing through a Ni-NTA column in the absence (−TCEP) or presence (+TCEP) of TCEP. Lane 1: GFP(-21) positive control; 2: molecular weight marker for native PAGE; 3: empty TRAP-cage; 4: input [TRAP-cage with GFP(-21)]; 5 and 8: flow through; 6 and 9: wash; and 7 and 10: elution. Collected fractions were stained for protein (left) or analyzed by fluorescence detection (right, exct. 488 nm). The GFP signal visible in lane 10 of the right-side gel likely reflects GFP still bound to a TRAP ring. (b) Western blot of the gel in (a): collected fractions were subjected to SDS-PAGE followed by western blot <t>with</t> <t>anti-GFP</t> detection. Lane 1: GFP(-21) positive control; 2: molecular weight marker for SDS-PAGE; 3: empty TRAP-cage; 4: input (TRAP-cage with GFP); 5 and 8: flow through; 6 and 9: wash; and 7 and 10: elution. (c) Native PAGE gels showing encapsulation of GFP(-21) by unmodified TRAP-cage or TRAP-cage externally modified with Alexa-647 and PTD4. Lane 1: TRAP-cage with GFP(-21); 2: TRAP-cage with GFP(-21) decorated with Alexa-647; 3: TRAP-cage with GFP(-21) decorated with Alexa-647 and PTD4; and 4: molecular weight marker for native PAGE. Gels were stained for protein (upper panel) and analyzed by fluorescence detection of GFP (middle panel, exct. 488 nm) and Alexa-647 (bottom panel, exct. 647). Gels were imaged using a Biorad Chemidoc detector. (d) Negative stain TEM of TRAP-cage with GFP(-21) (left panel); TRAP-cage with GFP(-21) decorated with Alexa-647 (middle panel); and TRAP-cage with GFP(-21) decorated with Alexa-647 and PTD4 (right panel).
Goat Anti Gfp, supplied by Rockland Immunochemicals, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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RayBiotech inc mouse anti gfp
Filling and decoration of TRAP-cage. (a) Native PAGE gels showing purified TRAP-cage incubated with His-tagged <t>GFP(-21)</t> after passing through a Ni-NTA column in the absence (−TCEP) or presence (+TCEP) of TCEP. Lane 1: GFP(-21) positive control; 2: molecular weight marker for native PAGE; 3: empty TRAP-cage; 4: input [TRAP-cage with GFP(-21)]; 5 and 8: flow through; 6 and 9: wash; and 7 and 10: elution. Collected fractions were stained for protein (left) or analyzed by fluorescence detection (right, exct. 488 nm). The GFP signal visible in lane 10 of the right-side gel likely reflects GFP still bound to a TRAP ring. (b) Western blot of the gel in (a): collected fractions were subjected to SDS-PAGE followed by western blot <t>with</t> <t>anti-GFP</t> detection. Lane 1: GFP(-21) positive control; 2: molecular weight marker for SDS-PAGE; 3: empty TRAP-cage; 4: input (TRAP-cage with GFP); 5 and 8: flow through; 6 and 9: wash; and 7 and 10: elution. (c) Native PAGE gels showing encapsulation of GFP(-21) by unmodified TRAP-cage or TRAP-cage externally modified with Alexa-647 and PTD4. Lane 1: TRAP-cage with GFP(-21); 2: TRAP-cage with GFP(-21) decorated with Alexa-647; 3: TRAP-cage with GFP(-21) decorated with Alexa-647 and PTD4; and 4: molecular weight marker for native PAGE. Gels were stained for protein (upper panel) and analyzed by fluorescence detection of GFP (middle panel, exct. 488 nm) and Alexa-647 (bottom panel, exct. 647). Gels were imaged using a Biorad Chemidoc detector. (d) Negative stain TEM of TRAP-cage with GFP(-21) (left panel); TRAP-cage with GFP(-21) decorated with Alexa-647 (middle panel); and TRAP-cage with GFP(-21) decorated with Alexa-647 and PTD4 (right panel).
Mouse Anti Gfp, supplied by RayBiotech inc, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 94 stars, based on 1 article reviews
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97
ABclonal Biotechnology anti ha
Filling and decoration of TRAP-cage. (a) Native PAGE gels showing purified TRAP-cage incubated with His-tagged <t>GFP(-21)</t> after passing through a Ni-NTA column in the absence (−TCEP) or presence (+TCEP) of TCEP. Lane 1: GFP(-21) positive control; 2: molecular weight marker for native PAGE; 3: empty TRAP-cage; 4: input [TRAP-cage with GFP(-21)]; 5 and 8: flow through; 6 and 9: wash; and 7 and 10: elution. Collected fractions were stained for protein (left) or analyzed by fluorescence detection (right, exct. 488 nm). The GFP signal visible in lane 10 of the right-side gel likely reflects GFP still bound to a TRAP ring. (b) Western blot of the gel in (a): collected fractions were subjected to SDS-PAGE followed by western blot <t>with</t> <t>anti-GFP</t> detection. Lane 1: GFP(-21) positive control; 2: molecular weight marker for SDS-PAGE; 3: empty TRAP-cage; 4: input (TRAP-cage with GFP); 5 and 8: flow through; 6 and 9: wash; and 7 and 10: elution. (c) Native PAGE gels showing encapsulation of GFP(-21) by unmodified TRAP-cage or TRAP-cage externally modified with Alexa-647 and PTD4. Lane 1: TRAP-cage with GFP(-21); 2: TRAP-cage with GFP(-21) decorated with Alexa-647; 3: TRAP-cage with GFP(-21) decorated with Alexa-647 and PTD4; and 4: molecular weight marker for native PAGE. Gels were stained for protein (upper panel) and analyzed by fluorescence detection of GFP (middle panel, exct. 488 nm) and Alexa-647 (bottom panel, exct. 647). Gels were imaged using a Biorad Chemidoc detector. (d) Negative stain TEM of TRAP-cage with GFP(-21) (left panel); TRAP-cage with GFP(-21) decorated with Alexa-647 (middle panel); and TRAP-cage with GFP(-21) decorated with Alexa-647 and PTD4 (right panel).
Anti Ha, supplied by ABclonal Biotechnology, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Image Search Results


Filling and decoration of TRAP-cage. (a) Native PAGE gels showing purified TRAP-cage incubated with His-tagged GFP(-21) after passing through a Ni-NTA column in the absence (−TCEP) or presence (+TCEP) of TCEP. Lane 1: GFP(-21) positive control; 2: molecular weight marker for native PAGE; 3: empty TRAP-cage; 4: input [TRAP-cage with GFP(-21)]; 5 and 8: flow through; 6 and 9: wash; and 7 and 10: elution. Collected fractions were stained for protein (left) or analyzed by fluorescence detection (right, exct. 488 nm). The GFP signal visible in lane 10 of the right-side gel likely reflects GFP still bound to a TRAP ring. (b) Western blot of the gel in (a): collected fractions were subjected to SDS-PAGE followed by western blot with anti-GFP detection. Lane 1: GFP(-21) positive control; 2: molecular weight marker for SDS-PAGE; 3: empty TRAP-cage; 4: input (TRAP-cage with GFP); 5 and 8: flow through; 6 and 9: wash; and 7 and 10: elution. (c) Native PAGE gels showing encapsulation of GFP(-21) by unmodified TRAP-cage or TRAP-cage externally modified with Alexa-647 and PTD4. Lane 1: TRAP-cage with GFP(-21); 2: TRAP-cage with GFP(-21) decorated with Alexa-647; 3: TRAP-cage with GFP(-21) decorated with Alexa-647 and PTD4; and 4: molecular weight marker for native PAGE. Gels were stained for protein (upper panel) and analyzed by fluorescence detection of GFP (middle panel, exct. 488 nm) and Alexa-647 (bottom panel, exct. 647). Gels were imaged using a Biorad Chemidoc detector. (d) Negative stain TEM of TRAP-cage with GFP(-21) (left panel); TRAP-cage with GFP(-21) decorated with Alexa-647 (middle panel); and TRAP-cage with GFP(-21) decorated with Alexa-647 and PTD4 (right panel).

Journal: Biomacromolecules

Article Title: Artificial Protein Cage Delivers Active Protein Cargos to the Cell Interior

doi: 10.1021/acs.biomac.1c00630

Figure Lengend Snippet: Filling and decoration of TRAP-cage. (a) Native PAGE gels showing purified TRAP-cage incubated with His-tagged GFP(-21) after passing through a Ni-NTA column in the absence (−TCEP) or presence (+TCEP) of TCEP. Lane 1: GFP(-21) positive control; 2: molecular weight marker for native PAGE; 3: empty TRAP-cage; 4: input [TRAP-cage with GFP(-21)]; 5 and 8: flow through; 6 and 9: wash; and 7 and 10: elution. Collected fractions were stained for protein (left) or analyzed by fluorescence detection (right, exct. 488 nm). The GFP signal visible in lane 10 of the right-side gel likely reflects GFP still bound to a TRAP ring. (b) Western blot of the gel in (a): collected fractions were subjected to SDS-PAGE followed by western blot with anti-GFP detection. Lane 1: GFP(-21) positive control; 2: molecular weight marker for SDS-PAGE; 3: empty TRAP-cage; 4: input (TRAP-cage with GFP); 5 and 8: flow through; 6 and 9: wash; and 7 and 10: elution. (c) Native PAGE gels showing encapsulation of GFP(-21) by unmodified TRAP-cage or TRAP-cage externally modified with Alexa-647 and PTD4. Lane 1: TRAP-cage with GFP(-21); 2: TRAP-cage with GFP(-21) decorated with Alexa-647; 3: TRAP-cage with GFP(-21) decorated with Alexa-647 and PTD4; and 4: molecular weight marker for native PAGE. Gels were stained for protein (upper panel) and analyzed by fluorescence detection of GFP (middle panel, exct. 488 nm) and Alexa-647 (bottom panel, exct. 647). Gels were imaged using a Biorad Chemidoc detector. (d) Negative stain TEM of TRAP-cage with GFP(-21) (left panel); TRAP-cage with GFP(-21) decorated with Alexa-647 (middle panel); and TRAP-cage with GFP(-21) decorated with Alexa-647 and PTD4 (right panel).

Article Snippet: The membrane was blocked with 5% skimmed milk in Tris-buffered saline supplemented with 0.05% Tween 20 (TBS-T), followed by 1.5 h of incubation with the mouse monoclonal anti-GFP antibody (1:2500; St. John’s Laboratories, UK) and anti-mouse (1:5000, Thermo Fisher Scientific) secondary antibody conjugated with horse radish peroxidase.

Techniques: Clear Native PAGE, Purification, Incubation, Positive Control, Molecular Weight, Marker, Staining, Fluorescence, Western Blot, SDS Page, Encapsulation, Modification